Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex |
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Authors: | de Graaf Petra Zwart Wilbert T van Dijken Remco A J Deneka Magdalena Schulz Thomas K F Geijsen Niels Coffer Paul J Gadella Bart M Verkleij Arie J van der Sluijs Peter van Bergen en Henegouwen Paul M P |
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Affiliation: | Department of Molecular Cell Biology and Institute of Biomembranes, Utrecht University, The Netherlands. |
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Abstract: | Phosphatidylinositol 4-kinasebeta (PI4Kbeta) plays an essential role in maintaining the structural integrity of the Golgi complex. In a search for PI4Kbeta-interacting proteins, we found that PI4Kbeta specifically interacts with the GTP-bound form of the small GTPase rab11. The PI4Kbeta-rab11 interaction is of functional significance because inhibition of rab11 binding to PI4Kbeta abolished the localization of rab11 to the Golgi complex and significantly inhibited transport of vesicular stomatitis virus G protein from the Golgi complex to the plasma membrane. We propose that a novel function of PI4Kbeta is to act as a docking protein for rab11 in the Golgi complex, which is important for biosynthetic membrane transport from the Golgi complex to the plasma membrane. |
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